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本文以ＧＳＴ－ＵＶＳ．２抗体和卵黄膜为检测手段，采用凝胶过滤和离子交换等方法将非洲爪蟾（Ｘｅｎｏｐｕｓｌａｅｖｉｓ）孵化酶纯化了９０倍以上，并研究了其酶活性和生化特性。实验发现，孵化酶分子量为６０ｋＤ，有很强的蛋白酶活性和卵黄膜溶解活性；它很不稳定，在纯化时极易降解为４０ｋＤ分子，４０ｋＤ分子没有卵黄膜溶解活性，但仍有很强的蛋白酶活性。４０ｋＤ分子很可能只代表６０ｋＤ分子中的蛋白酶功能区，而丢失了两个ＣＵＢ重复区。孵化酶对ＥＤＴＡ和金属离子非常敏感、又为ｐ－ＡＰＭＳＦ等胰蛋白酶抑制剂所强烈抑制，表明它是属于胰蛋白酶类型的一种金属蛋白酶。其特异性ＭＣＡ－底物为Ｂｏｃ－Ｌｅｕ－Ｇｌｙ－Ａｒｇ－ＭＣＡ。
This article to GST-UVS. 2 antibody and yolk membrane as the detection means, the Xenopus laevis hatch enzyme was purified by 90 times or more using gel filtration and ion exchange method, and its enzymatic activity and biochemical characteristics were studied. It was found that the molecular weight of the hatching enzyme was 60 kD, which showed strong protease activity and yolk membrane lysis activity. It was very unstable and easily degraded to 40 kD molecules during purification. The 40 kD molecule did not have yolk membrane lysis activity but still had strong Protease activity. It is likely that the 40 kD molecule represents only the protease domain in the 60 kD molecule and two CUB repeats are missing. Hatching enzyme is very sensitive to EDTA and metal ions and is strongly inhibited by trypsin inhibitors such as p-APMSF, indicating that it is a type of metalloproteinase belonging to the trypsin type. Its specific MCA-substrate is Boc-Leu-Gly-Arg-MCA.